ID   CRYD_VIBPA              Reviewed;         445 AA.
AC   Q87JP5;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Cryptochrome DASH;
GN   Name=cry; OrderedLocusNames=VPA0203;
OS   Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=223926;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIMD 2210633;
RX   PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA   Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA   Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA   Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT   "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT   distinct from that of V. cholerae.";
RL   Lancet 361:743-749(2003).
CC   -!- FUNCTION: May have a photoreceptor function. Binds DNA; probably
CC       functions as a transcriptional repressor (By similarity).
CC       {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC       Note=Binds 1 FAD per subunit. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate;
CC         Xref=ChEBI:CHEBI:15636; Evidence={ECO:0000250};
CC       Note=Binds 1 5,10-methenyltetrahydrofolate (MTHF) per subunit.
CC       {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the DNA photolyase class-1 family.
CC       {ECO:0000305}.
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DR   EMBL; BA000032; BAC61546.1; -; Genomic_DNA.
DR   RefSeq; NP_799713.1; NC_004605.1.
DR   RefSeq; WP_005479934.1; NC_004605.1.
DR   AlphaFoldDB; Q87JP5; -.
DR   SMR; Q87JP5; -.
DR   STRING; 223926.28808341; -.
DR   EnsemblBacteria; BAC61546; BAC61546; BAC61546.
DR   GeneID; 1190891; -.
DR   KEGG; vpa:VPA0203; -.
DR   PATRIC; fig|223926.6.peg.3158; -.
DR   eggNOG; COG0415; Bacteria.
DR   HOGENOM; CLU_010348_6_2_6; -.
DR   OMA; NWNYTAG; -.
DR   Proteomes; UP000002493; Chromosome 2.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003913; F:DNA photolyase activity; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR   Gene3D; 3.40.50.620; -; 1.
DR   InterPro; IPR014133; Cry_DASH.
DR   InterPro; IPR036134; Crypto/Photolyase_FAD-like_sf.
DR   InterPro; IPR036155; Crypto/Photolyase_N_sf.
DR   InterPro; IPR005101; Cryptochr/Photolyase_FAD-bd.
DR   InterPro; IPR002081; Cryptochrome/DNA_photolyase_1.
DR   InterPro; IPR006050; DNA_photolyase_N.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   PANTHER; PTHR11455; PTHR11455; 1.
DR   Pfam; PF00875; DNA_photolyase; 1.
DR   Pfam; PF03441; FAD_binding_7; 1.
DR   PRINTS; PR00147; DNAPHOTLYASE.
DR   SUPFAM; SSF48173; SSF48173; 1.
DR   SUPFAM; SSF52425; SSF52425; 1.
DR   TIGRFAMs; TIGR02765; crypto_DASH; 1.
DR   PROSITE; PS51645; PHR_CRY_ALPHA_BETA; 1.
PE   3: Inferred from homology;
KW   Chromophore; DNA-binding; FAD; Flavoprotein; Reference proteome; Repressor;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..445
FT                   /note="Cryptochrome DASH"
FT                   /id="PRO_0000235313"
FT   DOMAIN          4..137
FT                   /note="Photolyase/cryptochrome alpha/beta"
SQ   SEQUENCE   445 AA;  51570 MW;  87C7FF0430F17E41 CRC64;
     MKKKIGLYWF TFDLRLHDNS LLVDASSFLD ELVCLYCRPS VTPFLHHFAQ EVTLGRARQK
     FIDASLCELN DALGQLGQRL WTLDLPPYQA LKYAIQYLSV THLYSDAMAG SDEQSILHKL
     QDEYPHLVIV QHSVRSLFDE SKLPFTLPDL PETFTQFRKC VEGIDIAHPI DAPSRLPPMP
     KGAQLPTLSS FYFDESALFS GGEWSGLAHC RRYFFSGLAS SYKETRNGLD GMAYSTKFSP
     WLALGCVSPR MIHAMLKQYE QTQGANDSTY WIYFELLWRE YFYWYARCYQ QRLFRFGGIR
     NQPPLTSFYA HRFQQWKNGT TPYPIVNACM HQLNHTGYMS NRGRQLVASC LVHELGLDWR
     YGAAYFETQL IDYDVGSNWG NWQYLAGVGA DPRGSRQFNL EKQTQMYDPN HEFIERWQGR
     DSRAQQDVVD MVGWPITTQQ ENGDK